GPD1_YEAST
ID GPD1_YEAST Reviewed; 391 AA.
AC Q00055; A5YWB0; D6VRW8; Q6J5J2; Q6J5J5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 1;
DE EC=1.1.1.8 {ECO:0000269|PubMed:8196651};
GN Name=GPD1; Synonyms=DAR1, HOR1, OSG1; OrderedLocusNames=YDL022W;
GN ORFNames=D2830;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-49.
RX PubMed=7934860; DOI=10.1111/j.1365-2958.1993.tb00980.x;
RA Larsson K., Ansell R., Eriksson P., Adler L.;
RT "A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements
RT an osmosensitive mutant of Saccharomyces cerevisiae.";
RL Mol. Microbiol. 10:1101-1111(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8196651; DOI=10.1128/mcb.14.6.4135-4144.1994;
RA Albertyn J., Hohmann S., Thevelein J.M., Prior B.A.;
RT "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for
RT growth under osmotic stress in Saccharomyces cerevisiae, and its expression
RT is regulated by the high-osmolarity glycerol response pathway.";
RL Mol. Cell. Biol. 14:4135-4144(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Diastaticus / ATCC 62933 / NRC 5704 / J132b;
RX PubMed=7961476; DOI=10.1128/jb.176.22.7091-7095.1994;
RA Wang H.T., Rahaim P., Robbins P., Yocum R.R.;
RT "Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1
RT gene encoding a glycerol-3-phosphate dehydrogenase.";
RL J. Bacteriol. 176:7091-7095(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-16; ALA-143; PRO-164;
RP SER-183; SER-225 AND VAL-256.
RC STRAIN=FHS, and WFB;
RA Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.;
RT "Research on the mechanism of osmotolerance and thermotolerance of yeast.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fu C., Zheng D.;
RT "The effects of co-expression of ScGPD1 and AtNHX1 on the salt tolerance of
RT yeast.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
RX PubMed=1676389; DOI=10.1016/0378-1119(91)90228-4;
RA Sleep D., Ogden J.E., Roberts N.A., Goodey A.R.;
RT "Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-
RT phosphate dehydrogenase (GUT2) promoter.";
RL Gene 101:89-96(1991).
RN [9]
RP PROTEIN SEQUENCE OF 2-19 AND 271-278, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15210723; DOI=10.1074/jbc.m403310200;
RA Valadi A., Granath K., Gustafsson L., Adler L.;
RT "Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast
RT isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains
RT their different contributions to redox-driven glycerol production.";
RL J. Biol. Chem. 279:39677-39685(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP INDUCTION.
RX PubMed=15773992; DOI=10.1111/j.1365-2958.2005.04533.x;
RA Aguilera J., Rodriguez-Vargas S., Prieto J.A.;
RT "The HOG MAP kinase pathway is required for the induction of methylglyoxal-
RT responsive genes and determines methylglyoxal resistance in Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 56:228-239(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the production and accumulation of glycerol during
CC hyperosmotic stress conditions. Glycerol acts as a osmoregulator that
CC prevents loss of water and turgor of the cells.
CC {ECO:0000269|PubMed:8196651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8; Evidence={ECO:0000269|PubMed:8196651};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15210723}.
CC Peroxisome {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15210723}.
CC -!- INDUCTION: By osmotic stress and by methylglyoxal in a HOG pathway-
CC dependent manner. {ECO:0000269|PubMed:15773992,
CC ECO:0000269|PubMed:8196651}.
CC -!- MISCELLANEOUS: Present with 807 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be GUT2, the FAD-dependent glycerol-
CC 3-phosphate dehydrogenase. {ECO:0000305|PubMed:1676389}.
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DR EMBL; Z24454; CAA80827.1; -; Genomic_DNA.
DR EMBL; X76859; CAA54189.1; -; Genomic_DNA.
DR EMBL; U04621; AAA64936.1; -; Genomic_DNA.
DR EMBL; AY598965; AAT27375.1; -; Genomic_DNA.
DR EMBL; AY598968; AAT27378.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88337.1; -; Genomic_DNA.
DR EMBL; Z74071; CAA98582.1; -; Genomic_DNA.
DR EMBL; EF596737; ABQ58864.1; -; Genomic_DNA.
DR EMBL; M38740; AAA18631.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11828.1; -; Genomic_DNA.
DR PIR; S40059; S40059.
DR RefSeq; NP_010262.1; NM_001180081.1.
DR PDB; 4FGW; X-ray; 2.45 A; A/B=1-391.
DR PDBsum; 4FGW; -.
DR AlphaFoldDB; Q00055; -.
DR SMR; Q00055; -.
DR BioGRID; 32033; 143.
DR DIP; DIP-6393N; -.
DR IntAct; Q00055; 4.
DR MINT; Q00055; -.
DR STRING; 4932.YDL022W; -.
DR iPTMnet; Q00055; -.
DR MaxQB; Q00055; -.
DR PaxDb; Q00055; -.
DR PRIDE; Q00055; -.
DR TopDownProteomics; Q00055; -.
DR EnsemblFungi; YDL022W_mRNA; YDL022W; YDL022W.
DR GeneID; 851539; -.
DR KEGG; sce:YDL022W; -.
DR SGD; S000002180; GPD1.
DR VEuPathDB; FungiDB:YDL022W; -.
DR eggNOG; KOG2711; Eukaryota.
DR GeneTree; ENSGT00390000003114; -.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; Q00055; -.
DR OMA; FIHKVCD; -.
DR BioCyc; MetaCyc:YDL022W-MON; -.
DR BioCyc; YEAST:YDL022W-MON; -.
DR BRENDA; 1.1.1.8; 984.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR ChiTaRS; GPD1; yeast.
DR PRO; PR:Q00055; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q00055; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IMP:SGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006973; P:intracellular accumulation of glycerol; IMP:SGD.
DR GO; GO:0006116; P:NADH oxidation; IMP:SGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:SGD.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; NAD;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9"
FT CHAIN 2..391
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 1"
FT /id="PRO_0000138100"
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 41..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 310..311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT BINDING 339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P21695"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT VARIANT 16
FT /note="N -> D (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 143
FT /note="S -> A (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 164
FT /note="L -> P (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 183
FT /note="N -> S (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 225
FT /note="P -> S (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 256
FT /note="E -> V (in strain: WFB)"
FT /evidence="ECO:0000269|Ref.4"
FT CONFLICT 103..107
FT /note="DNLVA -> TIWLL (in Ref. 8; AAA18631)"
FT /evidence="ECO:0000305"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:4FGW"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:4FGW"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4FGW"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:4FGW"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:4FGW"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 235..257
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 261..283
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4FGW"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:4FGW"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:4FGW"
SQ SEQUENCE 391 AA; 42869 MW; F5F1F7F111F707D1 CRC64;
MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA KVVAENCKGY
PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT LPDNLVANPD LIDSVKDVDI
IVFNIPHQFL PRICSQLKGH VDSHVRAISC LKGFEVGAKG VQLLSSYITE ELGIQCGALS
GANIATEVAQ EHWSETTVAY HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI
CGALKNVVAL GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA
DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW LETCGSVEDF
PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D
